|Entry||Database: PDB / ID: 5urw|
|Title||Structure of the extended type VI secretion system sheath in Myxococcus xanthus|
|Keywords||PROTEIN TRANSPORT / T6SS / type IV secretion / protein machine / secretion system / sheath / contractile|
|Function/homology||Type VI secretion protein, EvpB/VC_A0108, tail sheath / Type VI secretion system, VipA, VC_A0107 or Hcp2 / Type VI secretion system, VipA, VC_A0107 or Hcp2 / Type VI secretion protein, EvpB/VC_A0108, tail sheath / Type VI secretion system effector, Hcp / Hcp1-like superfamily / Type VI secretion system effector, Hcp / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein|
Function and homology information
|Specimen source||Myxococcus xanthus / / bacteria|
|Method||Electron microscopy (24 Å resolution / Cell / Subtomogram averaging) / Transmission electron microscopy|
|Authors||Chang, Y.-W. / Rettberg, L.A. / Jensen, G.J.|
|Citation||Journal: EMBO Rep. / Year: 2017|
Title: structures of an intact type VI secretion system revealed by electron cryotomography.
Authors: Yi-Wei Chang / Lee A Rettberg / Davi R Ortega / Grant J Jensen
Abstract: The type VI secretion system (T6SS) is a versatile molecular weapon used by many bacteria against eukaryotic hosts or prokaryotic competitors. It consists of a cytoplasmic bacteriophage tail-like ...The type VI secretion system (T6SS) is a versatile molecular weapon used by many bacteria against eukaryotic hosts or prokaryotic competitors. It consists of a cytoplasmic bacteriophage tail-like structure anchored in the bacterial cell envelope via a cytoplasmic baseplate and a periplasmic membrane complex. Rapid contraction of the sheath in the bacteriophage tail-like structure propels an inner tube/spike complex through the target cell envelope to deliver effectors. While structures of purified contracted sheath and purified membrane complex have been solved, because sheaths contract upon cell lysis and purification, no structure is available for the extended sheath. Structural information about the baseplate is also lacking. Here, we use electron cryotomography to directly visualize intact T6SS structures inside cells. Using sub-tomogram averaging, we resolve the structure of the extended sheath and membrane-associated components including the baseplate. Moreover, we identify novel extracellular bacteriophage tail fiber-like antennae. These results provide new structural insights into how the extended sheath prevents premature disassembly and how this sophisticated machine may recognize targets.
Copyright: 2017 The Authors.
SummaryFull reportAbout validation report
|Date||Deposition: Feb 13, 2017 / Release: May 10, 2017|
Downloads & links
Mass: 18016.617 Da / Num. of mol.: 18
Source: (natural) Myxococcus xanthus (strain dk 1622) / / bacteria
Strain: DK 1622 / References: UniProt:Q1D305
Mass: 56188.469 Da / Num. of mol.: 18 / Source: (natural) Myxococcus xanthus / / bacteria / Strain: DK 1622 / References: UniProt:Q1D304
Mass: 18065.271 Da / Num. of mol.: 18 / Source: (natural) Myxococcus xanthus / / bacteria / Strain: DK 1622 / References: UniProt:Q1D303
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: CELL / Reconstruction method: SUBTOMOGRAM AVERAGING|
|Component||Name: Type VI secretion system / Type: COMPLEX / Entity ID: 1,||Source (natural)||Organism: Myxococcus xanthus DK 1622||Buffer solution||pH: 7||Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES||Vitrification||Cryogen name: ETHANE-PROPANE|
-Electron microscopy imaging
Model: Tecnai Polara / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI POLARA 300|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELD|
|Image recording||Electron dose: 1.5 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|CTF correction||Type: NONE|
|3D reconstruction||Resolution: 24 Å / Resolution method: OTHER / Number of particles: 687 / Symmetry type: POINT|
|EM volume selection||Number of tomograms: 29 / Number of volumes extracted: 687|
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